1 of 79
Definition
- Acid base catalysis = cleaves a peptide bond= Histidine acts as a
nucleophile to attack the hydroxyl group on the serine. This activates
the hydroxyl group on the serine to then attack the carbonyl on the
protein. Then the oxygen that was on the original carbonyl creates
hydrogen bonds to other residues on the active site.- Covalent
bonding = the covalent acyl-enzyme intermediate= After the peptide
bond is cleared, portions of substrate remains covalently bonded to
serine on the active site and stabilizes the intermediate and reduces
,transition state energy- Acid-base catalysis = disrupt the covalent
interactions between histidine and serine= reestabilishes the carbonyl
group and creates an acid
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Describe the basic mechanisms
Which of the following is an example
of serine proteases and
of enzyme regulation through
covalent catalysis; give an
covalent modification?
example of each
Apply how changes in enzyme
Compare the activities of glucokinase
concentration can be controlled by
and hexokinase with respect to the
changes in the rate of transcription or
Kms of each enzyme.
degradation.
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2 of 79
Term
Alpha helices and beta sheets are primarily stabilized by:
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H bonding Hydrogen bonding
, Polar covalent Dipole-dipole
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3 of 79
Term
Protein kinases phosphorylate proteins only at a certain hydroxyl
groups on amino acid side chains. All contain side chain hydroxyl
groups:
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Serine, Threonine, Tyrosine Asparagine And Glutamine
Lysine, Arginine, Histidine Allosteric Activation
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, 4 of 79
Definition
the higher concentration of reactants the more likely for a reaction to
occur
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Catalysis by proximity Catalysis by strain
Covalent catalysis Acid-base catalysis
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5 of 79
Term
Transamination is the first step in amino acid metabolism and it
involves:
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The transfer of an amine group
The synthesis of amino acids from
from an amino acid to a keto
simple sugars.
acid.
Definition
- Acid base catalysis = cleaves a peptide bond= Histidine acts as a
nucleophile to attack the hydroxyl group on the serine. This activates
the hydroxyl group on the serine to then attack the carbonyl on the
protein. Then the oxygen that was on the original carbonyl creates
hydrogen bonds to other residues on the active site.- Covalent
bonding = the covalent acyl-enzyme intermediate= After the peptide
bond is cleared, portions of substrate remains covalently bonded to
serine on the active site and stabilizes the intermediate and reduces
,transition state energy- Acid-base catalysis = disrupt the covalent
interactions between histidine and serine= reestabilishes the carbonyl
group and creates an acid
Give this one a try later!
Describe the basic mechanisms
Which of the following is an example
of serine proteases and
of enzyme regulation through
covalent catalysis; give an
covalent modification?
example of each
Apply how changes in enzyme
Compare the activities of glucokinase
concentration can be controlled by
and hexokinase with respect to the
changes in the rate of transcription or
Kms of each enzyme.
degradation.
Don't know?
2 of 79
Term
Alpha helices and beta sheets are primarily stabilized by:
Give this one a try later!
H bonding Hydrogen bonding
, Polar covalent Dipole-dipole
Don't know?
3 of 79
Term
Protein kinases phosphorylate proteins only at a certain hydroxyl
groups on amino acid side chains. All contain side chain hydroxyl
groups:
Give this one a try later!
Serine, Threonine, Tyrosine Asparagine And Glutamine
Lysine, Arginine, Histidine Allosteric Activation
Don't know?
, 4 of 79
Definition
the higher concentration of reactants the more likely for a reaction to
occur
Give this one a try later!
Catalysis by proximity Catalysis by strain
Covalent catalysis Acid-base catalysis
Don't know?
5 of 79
Term
Transamination is the first step in amino acid metabolism and it
involves:
Give this one a try later!
The transfer of an amine group
The synthesis of amino acids from
from an amino acid to a keto
simple sugars.
acid.
